This family has 22 members: 2 Arabidopsis thaliana, 2 Caenorhabditis elegans, 2 Danio rerio, 2 Dictyostelium discoideum, 2 Drosophila melanogaster, 1 Escherichia coli, 1 Gallus gallus, 2 Homo sapiens, 4 Mus musculus, 2 Rattus norvegicus, 1 Saccharomyces cerevisiae, 1 Schizosaccharomyces pombe.
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| Organism | Protein (Synonyms) | Description | AmiGO |
|---|---|---|---|
| A. thaliana | NCBI:NP_179395.1 · TAIR:locus:2060922 (T27K22_9 · T27K22.9 · AT2G18040 · PIN1AT) | PROLYL CIS/TRANS ISOMERASE · PEPTIDYLPROLYL CIS/TRANS ISOMERASE, NIMA-INTERACTING 1 |  |
| A. thaliana | NCBI:NP_564250.1 · TAIR:locus:2197970 (AT1G26550 · T1K7_8 · T1K7.8) | | |
| C. elegans | WB:WBGene00022448 (Y110A2AL.13) · UniProtKB:Q9N492 | | |
| C. elegans | WB:WBGene00012996 (Y48C3A.16) · UniProtKB:Q9NAF9 | | |
| D. rerio | ENSEMBL:ENSDARP00000096689 | ||
| D. rerio | ZFIN:ZDB-GENE-050522-117 (zgc:110008) · UniProtKB:Q503Y7 | | |
| D. discoideum | UniProtKB:Q54Z53 · dictyBase:DDB_G0277775 (DDB_G0277775) | Similar to Y48C3A.16.p. | |
| D. discoideum | UniProtKB:Q55EZ0 · dictyBase:DDB_G0268618 (pinA) | PinA (Fragment). | |
| D. melanogaster | FB:FBgn0015379 (CG17051 · dod · Pin1 · dodo) · UniProtKB:P54353 | | |
| D. melanogaster | FB:FBgn0039305 (CG11858 · BcDNA:RH66629) · UniProtKB:Q9VBU4 | | |
| E. coli | UniProtKB:P0A9L5 · ECOLI:EG12352-MONOMER (b3775 · PpiC · ECK3767 · parvA · ppiC) | peptidyl-prolyl cis-trans isomerase C (rotamase C) | |
| G. gallus | NCBI:XP_420136 · ENTREZ:422134 | ||
| H. sapiens | ENSEMBL:ENSG00000127445 · UniProtKB:Q13526 (PIN1 · Q13526 · PIN1_HUMAN · IPI00013723) | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | |
| H. sapiens | ENSEMBL:ENSG00000102309 · UniProtKB:Q9Y237 (IPI00006658 · Q9Y237 · PIN4 · PIN4_HUMAN) | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 | |
| M. musculus | NCBI:XP_981610 · MGI:MGI:3780035 | ||
| M. musculus | NCBI:XP_897983 · MGI:MGI:3643618 | ||
| M. musculus | UniProtKB:Q9QUR7 · MGI:MGI:1346036 (Pin1 · D9Bwg1161e) | protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 | |
| M. musculus | UniProtKB:Q9CWW6 · MGI:MGI:1916963 (EPVH · Par14 · Pin4) | protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin) | |
| R. norvegicus | NCBI:XP_216609 · RGD:1310299 (Pin1) | peptidylprolyl cis/trans isomerase, NIMA-interacting 1 | |
| R. norvegicus | NCBI:XP_001070406 · RGD:1590326 (LOC684441) | similar to Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (Rotamase Pin4) (PPIase Pin4) | |
| S. cerevisiae | UniProtKB:P22696 · SGD:S000003778 (PTF1 · PIN1 · YJR017C · ESS1) | Peptidylprolyl-cis/trans-isomerase (PPIase) specific for phosphorylated serine and threonine residues N-terminal to proline | |
| S. pombe | UniProtKB:O74448 · GeneDB_Spombe:SPCC16C4.03 (SPCC16C4.03 · pin1) | peptidyl-prolyl cis-trans isomerase Pin1 | |
| Protein | Publication | Curator Notes | |
|---|---|---|---|
| UniProtKB:P22696 · SGD:S000003778 |  11118438 Yao JL, et al. Functional conservation of phosphorylation-specific prolyl isomerases in plants. J Biol Chem. 2001 Apr 27;276(17):13517-23. | The A. thaliana protein AT2G18040.1 complements a homologous mutation in S. cerevisiae. | |
| UniProtKB:P22696 · SGD:S000003778 | 11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9. | The D. lanata protein DlPar13 complements a homologous mutation in S. cerevisiae. | |
| UniProtKB:P22696 · SGD:S000003778 | 15870468 Ren P, et al. The Ess1 prolyl isomerase is dispensable for growth but required for virulence in Cryptococcus neoformans. Microbiology. 2005 May;151(Pt 5):1593-605. | The C. neoformans protein Ess1 complements a homologous mutation in S. cerevisiae. The C. neoformins Ess1 gene has the GenBank id AF533511. Three complementation tests indicated that C. neoformans ESS1 encodes a bona fide functional homologue of S. cerevisiae ESS1. | |
| UniProtKB:P22696 · SGD:S000003778 | 11707530 Huang HK, et al. Isolation and characterization of the Pin1/Ess1p homologue in Schizosaccharomyces pombe. J Cell Sci. 2001 Oct;114(Pt 20):3779-88. | The S. pombe protein Pin1 complements a homologous mutation in S. cerevisiae. | |
| UniProtKB:P22696 · SGD:S000003778 | 11118438 Yao JL, et al. Functional conservation of phosphorylation-specific prolyl isomerases in plants. J Biol Chem. 2001 Apr 27;276(17):13517-23. | The M. domestica protein MdPin1 complements a homologous mutation in S. cerevisiae. MdPin1 has the GenBank accession id AF209200. | |
| UniProtKB:P22696 · SGD:S000003778 | 11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9. | The H. sapiens protein Q13526 complements a homologous mutation in S. cerevisiae. | |
| UniProtKB:P22696 · SGD:S000003778 | 11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9. | The H. sapiens protein Q9Y237 does not complement a homologous mutation in S. cerevisiae. Human Par14/Pin4 (Q9Y237) was shown not to complement a yeast ess1 mutant, whereas human Pin1 (Q13526) did complement the yeast ess1 mutant indicating that it is likely the functional homolog of yeast Ess1p. | |
| UniProtKB:P22696 · SGD:S000003778 | 11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9. | The H. sapiens protein PIN4 does not complement a homologous mutation in S. cerevisiae. | |
| UniProtKB:P22696 · SGD:S000003778 | 11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9. | The H. sapiens protein PIN1 complements a homologous mutation in S. cerevisiae. |
| Description | Suffix |
|---|---|
| Sequences in this family | .fasta |
| mafft aligned Fasta file | .afasta |
| phyml newick file | .newick |
| Notung rooted & rearranged newick file | .newick.rooting.0.rearrange.0 |
| Notung Homolog Table | .newick.rooting.0.rearrange.0.homologs.csv |
| SGD Disease Papers (1) | |
|---|---|
| UniProtKB:P22696 · SGD:S000003778 | 18844375 Bailey ML, et al. (2008) The dual histidine motif in the active site of Pin1 has a structural rather than catalytic role. Biochemistry 47(44):11481-9 |